ID D7M615_ARALL Unreviewed; 512 AA.
AC D7M615;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Protoporphyrinogen oxidase {ECO:0000256|ARBA:ARBA00012867, ECO:0000256|RuleBase:RU367069};
DE EC=1.3.3.4 {ECO:0000256|ARBA:ARBA00012867, ECO:0000256|RuleBase:RU367069};
GN ORFNames=ARALYDRAFT_488256 {ECO:0000313|EMBL:EFH49915.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC to form protoporphyrin-IX. {ECO:0000256|ARBA:ARBA00002600,
CC ECO:0000256|RuleBase:RU367069}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX;
CC Xref=Rhea:RHEA:25576, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; EC=1.3.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000672,
CC ECO:0000256|RuleBase:RU367069};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU367069};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU367069};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005073, ECO:0000256|RuleBase:RU367069}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU367069}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Protoporphyrinogen oxidase subfamily.
CC {ECO:0000256|ARBA:ARBA00010551, ECO:0000256|RuleBase:RU367069}.
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DR EMBL; GL348718; EFH49915.1; -; Genomic_DNA.
DR RefSeq; XP_002873656.1; XM_002873610.1.
DR AlphaFoldDB; D7M615; -.
DR STRING; 81972.D7M615; -.
DR EnsemblPlants; fgenesh2_kg.6__1390__AT5G14220.1; fgenesh2_kg.6__1390__AT5G14220.1; fgenesh2_kg.6__1390__AT5G14220.1.
DR Gramene; fgenesh2_kg.6__1390__AT5G14220.1; fgenesh2_kg.6__1390__AT5G14220.1; fgenesh2_kg.6__1390__AT5G14220.1.
DR eggNOG; KOG1276; Eukaryota.
DR HOGENOM; CLU_009629_3_2_1; -.
DR OrthoDB; 65450at2759; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.3110.10; protoporphyrinogen ix oxidase, domain 3; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR NCBIfam; TIGR00562; proto_IX_ox; 1.
DR PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR PANTHER; PTHR42923:SF3; PROTOPORPHYRINOGEN OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU367069};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU367069};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133,
KW ECO:0000256|RuleBase:RU367069};
KW Oxidoreductase {ECO:0000256|RuleBase:RU367069};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU367069};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 28..496
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 224..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 56021 MW; 8874C0FF08AD88C0 CRC64;
MESGAVGDHD TKFESISGKR VAVVGAGVSG LAAAYKLKSR GLNVTVFEAD ERAGGKLTSV
MQNGLIWDQG ANTMTEAEPE VGSLLDDLGL RDKQQFPISQ KKRYIVRNGL PMMLPTNPIE
LVTSSVLSTQ AKIQILLEPF LWKKNDSSSK VSDASAEESV SGFFQRHFGQ EVVDYLIDPF
VGGTSAADPD SLSMKHSFPD LWNVEKSFGS IIVGAIRTKL AAKGGKSGEA KSSPGTKRGS
RRSFSFKGGM QILPDMLCKS LSHDEINLDS KVLSLSYNSG SRQENWSLSC VSHNETQRQN
LHYDAVVMTA PLCNVKEMKV TKGGQPFLLN FLPEINYMPL SVLITTFTKE KVKRPLEGFG
VLIPSKEKKH GFKTLGTLFS SMMFPDRCPS DLHLYTTFIG GSRNQELAKA STDELKQVVT
SDLQRLLGVE GEPVSVNHYY WRKAFPLYDS SYGSVMEAID KMEKDLPGFF YAGNHRGGLS
IGKSIASGCK AADLVISYLE SCSNDKKPDE SL
//